Alias |
26S protease subunit S5a,26S proteasome non ATPase regulatory subunit 4,26S proteasome non-ATPase regulatory subunit 4,26S proteasome regulatory subunit rpn10,26S proteasome regulatory subunit S5A,AF 1,AF,AF1,Angiocidin,Antisecretory factor 1,ASF,DS5a,MCB 1,MCB1,Multiubiquitin chain binding protein,Multiubiquitin chain-binding protein,OTTHUMP00000059963,Prosome macropain,Proteasome (prosome macropain) 26S subunit non ATPase 4,Proteasome 26S non ATPase subunit 4,Proteasome 26S subunit non ATPase 4,PSMD 4,Psmd4,PSMD4,pUB R5,pUBR5,Rpn 10,Rpn10,RPN10 homolog,S5A,S5a/antisecretory factor protein |
Background |
The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the non-ATPase subunits of the 19S regulator lid. Pseudogenes have been identified on chromosomes 10 and 21. |